DBP7_KLULA
ID DBP7_KLULA Reviewed; 740 AA.
AC Q6CK32;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=ATP-dependent RNA helicase DBP7;
DE EC=3.6.4.13;
GN Name=DBP7; OrderedLocusNames=KLLA0F13926g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: ATP-binding RNA helicase involved in the biogenesis of 60S
CC ribosomal subunits and is required for the normal formation of 25S and
CC 5.8S rRNAs. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CC -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD box
CC family of RNA helicases and controls ATP binding and hydrolysis.
CC -!- MISCELLANEOUS: Present with 1460 molecules/cell in log phase SD medium.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX31/DBP7
CC subfamily. {ECO:0000305}.
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DR EMBL; CR382126; CAG98415.1; -; Genomic_DNA.
DR RefSeq; XP_455707.1; XM_455707.1.
DR AlphaFoldDB; Q6CK32; -.
DR SMR; Q6CK32; -.
DR STRING; 28985.XP_455707.1; -.
DR EnsemblFungi; CAG98415; CAG98415; KLLA0_F13926g.
DR GeneID; 2894880; -.
DR KEGG; kla:KLLA0_F13926g; -.
DR eggNOG; KOG0348; Eukaryota.
DR HOGENOM; CLU_003041_26_2_1; -.
DR InParanoid; Q6CK32; -.
DR OMA; AVHIKAD; -.
DR Proteomes; UP000000598; Chromosome F.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:EnsemblFungi.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR025313; DUF4217.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF13959; DUF4217; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01178; DUF4217; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 3: Inferred from homology;
KW ATP-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Reference proteome; Ribosome biogenesis; RNA-binding; rRNA processing.
FT CHAIN 1..740
FT /note="ATP-dependent RNA helicase DBP7"
FT /id="PRO_0000232257"
FT DOMAIN 182..376
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 414..607
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 695..721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 149..178
FT /note="Q motif"
FT MOTIF 311..314
FT /note="DEAD box"
FT COMPBIAS 37..64
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 195..202
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 740 AA; 82682 MW; BBC7EF9B2ADEC4C2 CRC64;
MSFNDDDDGM LLNFTTDVSD ASETVSRGKI TGGKWKDRRK AKMMMEGRKP RVRGEKRPLE
SDGAPTFEEL EASSSNSTSA QAPVEPKRSR FDNSSNVEQP ARVTQPLQLN SQIVSSLFTS
SRNIDTVTNS NAHDEKAEVT YSNAPLVGDT FDSFGITDTM VSHLNVKMKI SKPTKIQKLV
IPPFLQAQND LFIHAQTGSG KTLAFLLPIF QSILSLGQNI TRQSGCFALV VTPTRELANQ
IYQVTSELAQ CCHFLVPCLL IGGERKKSEK ARLRKGANFI IGTPGRVLDH LQNTKVIKEQ
LAPSLRYVVL DEGDKLMELG FEETLKEILN IIHGIDIDTH QFPKLPKRIL HVLCSATVKG
NVTKLGNVTL QNYKLISSGQ KQTETTTVPD QLLQKIVIVP PKLRLVTLAG SLTTITQKHY
KEGSKSDVTR TIVFLSCSDS VDFHYEVFSS HDGNHRGLVG DTARLLTKGN SILPCFNDTD
DPNVICYKLH GSLSQQTRTA TLKHFATNND ATKGKHLILF CTDVASRGLD LPHVSTVIEM
DPPFAVEDHL HRIGRTARAG CEGESLLFLL PGEEEGYMDY IKPYHPKGWK LLTYDEQVLR
PAFEGLNVRR TDKKKEDWDK HEAQAWDNNA TTWHLNVERR VIEDSHFKEL AVKGYMSHIR
AYATHLSIEK KFFNLKCLHL GHLAKSFALR ERPKSMGLQQ GKAGAAAAAS QKKPKEDSKS
KMLRMAKMAM RQSNDEFNFA
